1kkb: Difference between revisions

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-[[Image:1kkb.gif|left|200px]]
- {{Structure
+==Complex of Escherichia coli Adenylosuccinate Synthetase with IMP and Hadacidin==
-|PDB= 1kkb |SIZE=350|CAPTION= <scene name='initialview01'>1kkb</scene>, resolution 2.6&Aring;
+<StructureSection load='1kkb' size='340' side='right'caption='[[1kkb]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HAD:(CARBOXYHYDROXYAMINO)ETHANOIC+ACID'>HAD</scene> and <scene name='pdbligand=IMP:INOSINIC ACID'>IMP</scene>
+<table><tr><td colspan='2'>[[1kkb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKB FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kkb OCA], [https://pdbe.org/1kkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kkb RCSB], [https://www.ebi.ac.uk/pdbsum/1kkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kkb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PURA_ECOLI PURA_ECOLI] Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[HAMAP-Rule:MF_00011]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kk/1kkb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kkb ConSurf].
+<div style="clear:both"></div>
-'''Complex of Escherichia coli Adenylosuccinate Synthetase with IMP and Hadacidin'''
+==See Also==
+*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-A complete set of substrate/substrate analogs of adenylosuccinate synthetase from Escherichia coli induces dimer formation and a transition from a disordered to an ordered active site. The most striking of the ligand-induced effects is the movement of loop 40-53 by up to 9 A. Crystal structures of the partially ligated synthetase, which either combine IMP and hadacidin or IMP, hadacidin, and Mg(2+)-pyrophosphate, have ordered active sites, comparable with the fully ligated enzyme. More significantly, a crystal structure of the synthetase with IMP alone exhibits a largely ordered active site, which includes the 9 A movement of loop 40-53 but does not include conformational adjustments to backbone carbonyl 40 (Mg(2+) interaction element) and loop 298-304 (L-aspartate binding element). Interactions involving the 5'-phosphoryl group of IMP evidently trigger the formation of salt links some 30 A away. The above provides a structural basis for ligand binding synergism, effects on k(cat) due to mutations far from the site of catalysis, and the complete loss of substrate efficacy due to minor alterations of the 5'-phosphoryl group of IMP.
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Fromm HJ]]
-KKB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKB OCA].
+[[Category: Honzatko RB]]
+[[Category: Hou Z]]
-==Reference==
+[[Category: Wang W]]
-IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli., Hou Z, Wang W, Fromm HJ, Honzatko RB, J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11741996 11741996]
-[[Category: Adenylosuccinate synthase]]
-[[Category: Escherichia coli]]
-[[Category: Single protein]]
-[[Category: Fromm, H J.]]
-[[Category: Honzatko, R B.]]
-[[Category: Hou, Z.]]
-[[Category: Wang, W.]]
-[[Category: HAD]]
-[[Category: IMP]]
-[[Category: biosynthesis]]
-[[Category: gtp-hydrolysing enzyme]]
-[[Category: induced fit]]
-[[Category: ligase]]
-[[Category: purine nucleotide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:18:35 2008''